A generalizable method for the purification and biophysical characterization of bacterial membrane receptors
Federico Bosetto, Maria Zacharopoulou, Mark Bycroft, Monika Kish, Giovanna Zinzalla, Pamela J. E. Rowling, Stephen H. McLaughlin, Jonathan J. Phillips, Laura S. Itzhaki, Ioanna Mela · 2026
Read A generalizable method for the purification and biophysical characterization of bacterial membrane receptors by Federico Bosetto, Maria Zacharopoulou, Mark Bycroft, Monika Kish, Giovanna Zinzalla, Pamela J. E. Rowling, Stephen H. McLaughlin, Jonathan J. Phillips, Laura S. Itzhaki, Ioanna Mela (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13670019.txt.
Description
Bacteria wear receptors in their outer membrane that are vital but notoriously hard to pull out and study. Federico Bosetto and co-authors present a general recipe in a 2026 paper, worked out on a receptor that Pseudomonas uses to steal iron from blood pigment. The two working ends of that receptor can be made on their own in lab bacteria.
Each end was purified to a clean, well-folded state, checked by three kinds of measurement. The team then fused the ends and tested tag systems for keeping the fusion soluble. A double tag worked, while single tags left the protein clumped or chewed up. The folded map of the parts sets up future work on blocking the iron supply of this pathogen.
Catalog record
| CREATOR | Federico Bosetto, Maria Zacharopoulou, Mark Bycroft, Monika Kish, Giovanna Zinzalla, Pamela J. E. Rowling, Stephen H. McLaughlin, Jonathan J. Phillips, Laura S. Itzhaki, Ioanna Mela |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 64 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |